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BP: Fachverband Biologische Physik
BP 26: Posters II
BP 26.8: Poster
Thursday, February 28, 2008, 17:00–19:30, Poster A
Proteins under extreme conditions - new SAXS setup at beamline BL9 of DELTA synchrotron — •Christina Krywka1, Christian Sternemann1, Roland Winter2, and Metin Tolan1 — 1Fachbereich Physik, Universität Dortmund, D-44221 Dortmund, Germany — 2Fachbereich Physikalische Chemie, Universität Dortmund, D-44221 Dortmund, Germany
The biological activity and the chemical properties of proteins depend on the structure of the solvent and its thermodynamic parameters. Understanding the effects of cosolvents on the structure and dynamics of proteins is crucial for a deeper insight into protein stability, folding, aggregation and fibrillation processes. The latter play an important role in many conformational diseases, such as Alzheimer, Creutzfeldt-Jakob, and Parkinson. Recently, we could show that these fibrillation processes are strongly influenced by the type and concentration of cosolvents. In order to determine the effects of different types of cosolvents on the native and unfolded states of the model protein Staphylococcal Nuclease (SNase) we have performed Small-Angle-X-ray-Scattering (SAXS) measurements at temperature and pressure conditions where unfolding of the protein sets in. The experimental equipment which had to be developed in the course of the ongoing project comprises of a high-pressure, temperature controlled sample cell with the ability to perform SAXS-measurements at pressures up to 7 kbar in a wide temperature range (-15°C to 80°C). This contribution will provide an outline of recent high-pressure data of SNase and the experimental setup installed at the multi-purpose beamline BL9.